Studies on mammalian intestinal peroxidase

Kimura, Shioko; Jellinck, Peter H.

doi:10.1042/bj2050271

Cited by 32 publications

(28 citation statements)

References 37 publications

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“…However, this is significantly different from the value reported for human eosinophil enzyme where a native M , of 77000 or 71000 with two subunits of M , 58000 and 14000 or 52000 and 15000, respectively, has been reported [15, 161. The electrophoretic migration of the gastric peroxidase at acid pH indicates that it is a basic protein similar to the intestine, uterine and eosinophil enzymes [3,4,30]. The spectral properties of the native enzyme as well as its derivatives also bear close similarity with the above enzymes including lactoperoxidase [3,4,.…”

Section: Discussionmentioning

confidence: 89%

“…Gastric peroxidase has several properties similar to the intestinal [3], eosinophil [4] and uterine [30] peroxidase. It is now almost established that intestinal and uterine peroxidases are derived from the invading eosinophils [3,17,181.…”

Section: Discussionmentioning

confidence: 99%

“…The electrophoretic migration of the gastric peroxidase at acid pH indicates that it is a basic protein similar to the intestine, uterine and eosinophil enzymes [3,4,30]. The spectral properties of the native enzyme as well as its derivatives also bear close similarity with the above enzymes including lactoperoxidase [3,4,. The kl value of the gastric peroxidase (1.38 x lo7 M-' s-' ) is of the same order of magnitude as kl values reported for intestinal, uterine, eosinophil and lactoperoxidase [3,4,11,18,331.…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

“…It is now almost established that intestinal and uterine peroxidases are derived from the invading eosinophils [3,17,181. The M , of the rat gastric peroxidase (45 000 2000) is close to that of the rat intestinal, eosinophil and uterine peroxidase [3,4,301. However, this is significantly different from the value reported for human eosinophil enzyme where a native M , of 77000 or 71000 with two subunits of M , 58000 and 14000 or 52000 and 15000, respectively, has been reported [15, 161.…”

Section: Discussionmentioning

confidence: 99%

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Purification, characterization and origin of rat gastric peroxidase

Banerjee

1986

European Journal of Biochemistry

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A membrane-bound peroxidase (EC 1.1 1.1.7) from rat stomach has been solubilized by 0.2% cetyltrimethylammonium bromide in the presence of 1.2 M NH4Cl. The enzyme was purified 3355-fold to apparent homogeneity as judged by acid polyacrylamide gel electrophoresis and appears to be a cationic protein. In sodium dodecyl sulfate gel electrophoresis, the enzyme shows single polypeptide band of M , 45000. In gel permeation, the M , has been estimated as 47000. Spectral properties indicate the presence of Soret band at 412 nm which shifts to 425 nm on complexation with CN-and to 430 nm on reduction with dithionite. The velocity constant, kl for the reaction of the proxidase with H202 is 1.38 x lo7 M-' s-' and K,,, for H,O, is 0.1 mM. The enzyme contains active sulphydryl groups and is inhibited by sulphydryl reagents of which p-hydroxymercuribenzoate is more reactive than mersalyl or N-ethylmaleimide. The enzyme is very resistant to thermal denaturation up to 65°C and also to chaotropic reagents at least up to 2 M above which it is inactivated. The enzyme shows similarity with the intestinal eosinophil peroxidase as regards the molecular mass, spectral, kinetic and some of the catalytic properties. However, they differ significantly in terms of their interaction with fluoride ion, sulphydryl reagents, chaotropic reagent and also with the antiserum against the gastric peroxidase. Histochemically, the gastric peroxidase is shown to be localised in the gastric gland proper of the fundic stomach, rich in parietal and chief cells.After the suggestion of Rytomaa and Teir tha't all animal tissue peroxidases (except thyroid and myeloperoxidase) are contributed by the eosinophils [l], the properties of the peroxidases purified from various tissues have been compared [2 -161 in order to establish whether the enzyme is distinct and intrinsic to each tissue or it is derived from the contaminating eosinophils. Recently King et al. [17] and Olsen and Little [5] have shown that estrogen-induced peroxidase in rat uterus is mainly contributed by the eosinophils. The enzyme from pig and rat intestine has also been characterized and shown to have some similarities with eosinophil peroxidase [2, 31. Very recently we have established that rat intestinal peroxidase is not an endogenous enzyme and is mainly derived from the eosinophils accumulating in the core of the intestinal villi [18].The presence of a highly active peroxidase in mouse gastric mucosa and its cellular and subcellular localization was reported earlier from our labortory [19]. Recently we have shown that this enzyme in rat gastric mucosa is modulated by adrenal glucocorticoids [20]. However, it is not established yet whether gastric peroxidase is an enzyme intrinsic to the tissue or is contributed by the eosinophls, as in the case of intestinal peroxidase [18]. We have isolated homogeneous gastric peroxidase and its molecular, spectral, kinetic, catalytic and immunological properties have been studied and compared with those of the intestinal eosinophil peroxidase. The data...

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Purification, characterization and origin of rat gastric peroxidase

Banerjee

1986

European Journal of Biochemistry

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Influence of inflammatory cells and serum on the performance of implantable glucose sensors

Gerritsen

Jansen

Kros

et al. 2000

J. Biomed. Mater. Res.

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The objective of this investigation was to evaluate the influence of polymorphonuclear granulocytes on the performance of uncoated and cellulose acetate/Nafion coated amperometric glucose sensors in vitro. The response of these sensors was also investigated in serum. Uncoated and coated sensors showed lower sensitivities to glucose, with a significant drift in sensor output upon exposure to serum or leukocytes. Although the use of a coating resulted in higher sensitivity, the progressive loss of output was not completely prevented. Stimulated granulocytes were shown to excrete components, probably catalase and myeloperoxidase, which consumed the hydrogen peroxide formed by the oxidation of glucose. In addition, adsorbed serum proteins formed a diffusional barrier for glucose. Furthermore, serum was found to contain low-molecular weight components that alone inhibited glucose oxidase activity. Based on preliminary electrochemical results, we postulate that rabbit serum contains oxidizing substrates that compete with molecular oxygen for the acceptance of electrons from the oxidized enzyme. Consequently, future efforts should be aimed at elucidating the mechanisms involved in the interference of unknown serum components with electron transfer. In addition, further investigations have to be performed to develop an outer membrane that minimizes protein adsorption as well as the actions of inflammatory cells.

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Peroxidase

Springer Handbook of Enzymes

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Studies on mammalian intestinal peroxidase

Cited by 32 publications

References 37 publications

Purification, characterization and origin of rat gastric peroxidase

Purification, characterization and origin of rat gastric peroxidase

Influence of inflammatory cells and serum on the performance of implantable glucose sensors

Peroxidase

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